ISSN:
1423-0127
Schlagwort(e):
Fusarium sporotrichioides
;
Peptidyl-prolyl isomerase
;
Partial amino acid sequence
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Medizin
Notizen:
Abstract Peptidyl-proprylyl cis-trans isomerase (PPIase) activity was observed from crude extract ofFusarium sporotrichioides. Proteins from this fungi were separated by two-dimensional polyacrylamide gel electrophoresis and more than one thousand protein spots were separated. Two cytosolic PPIases were found by the N-terminal sequencing from the two separated spots. The N-terminal 41 residues of the major protein spot showed high sequence identity (63.4%) with PPIase fromNeurospora crassa. This protein was designated as PPIase a, having an apparent molecular mass of 20 kD and pI 7.0. The minor other protein spot, having a similar molecular mass but distinguishable pI 6.4, was also sequenced and the N-terminal twenty residues were almost identical to PPIase a and was designated as PPIase b.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF02255222
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